CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019410
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytosolic non-specific dipeptidase 
Protein Synonyms/Alias
 CNDP dipeptidase 2; Glutamate carboxypeptidase-like protein 1; Peptidase A 
Gene Name
 CNDP2 
Gene Synonyms/Alias
 CN2; CPGL; PEPA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9AALTTLFKYIDENQDacetylation[1]
24RYIKKLAKWVAIQSVubiquitination[2, 3]
68LVDIGKQKLPDGSEIubiquitination[4]
149NALEAYQKTGQEIPVubiquitination[5]
202DNYWLGKKKPCITYGubiquitination[6]
302ILLHSHKKDILMHRWubiquitination[4]
363QVTSYLTKKFAELRSubiquitination[7]
383VYMGHGGKPWVSDFSubiquitination[2, 3, 4, 6]
402LAGRRAMKTVFGVEPubiquitination[2, 3, 4, 6]
430TFQEATGKNVMLLPVubiquitination[4]
450GAHSQNEKLNRYNYIubiquitination[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Isoform 2 may be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. 
Sequence Annotation
 REGION 166 167 Substrate binding (By similarity).
 ACT_SITE 101 101 By similarity.
 ACT_SITE 166 166 Proton acceptor (By similarity).
 METAL 99 99 Manganese 2 (By similarity).
 METAL 132 132 Manganese 1 (By similarity).
 METAL 132 132 Manganese 2 (By similarity).
 METAL 167 167 Manganese 1 (By similarity).
 METAL 195 195 Manganese 2 (By similarity).
 METAL 445 445 Manganese 1 (By similarity).
 BINDING 195 195 Substrate; via carbonyl oxygen (By
 BINDING 228 228 Substrate; shared with homodimeric
 BINDING 330 330 Substrate; shared with homodimeric
 BINDING 343 343 Substrate (By similarity).
 BINDING 417 417 Substrate; via amide nitrogen and
 BINDING 445 445 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 9 9 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Carboxypeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
MAALTTLFKY IDENQDRYIK KLAKWVAIQS VSAWPEKRGE IRRMMEVAAA DVKQLGGSVE 60
LVDIGKQKLP DGSEIPLPPI LLGRLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE 120
RDGKLYGRGS TDDKGPVAGW INALEAYQKT GQEIPVNVRF CLEGMEESGS EGLDELIFAR 180
KDTFFKDVDY VCISDNYWLG KKKPCITYGL RGICYFFIEV ECSNKDLHSG VYGGSVHEAM 240
TDLILLMGSL VDKRGNILIP GINEAVAAVT EEEHKLYDDI DFDIEEFAKD VGAQILLHSH 300
KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPNMTP EVVGEQVTSY 360
LTKKFAELRS PNEFKVYMGH GGKPWVSDFS HPHYLAGRRA MKTVFGVEPD LTREGGSIPV 420
TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRYNYIEGT KMLAAYLYEV SQLKD 475 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004180; F:carboxypeptidase activity; TAS:Reactome.
 GO:0016805; F:dipeptidase activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0034701; F:tripeptidase activity; IEA:InterPro.
 GO:0006750; P:glutathione biosynthetic process; TAS:Reactome.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
Interpro
 IPR001261; ArgE/DapE_CS.
 IPR017153; GSH_degradosome_DUG1.
 IPR002933; Peptidase_M20.
 IPR011650; Peptidase_M20_dimer. 
Pfam
 PF07687; M20_dimer
 PF01546; Peptidase_M20 
SMART
  
PROSITE
 PS00758; ARGE_DAPE_CPG2_1
 PS00759; ARGE_DAPE_CPG2_2 
PRINTS